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Fig. 2 | Molecular Brain

Fig. 2

From: Amyloid β oligomers elicit mitochondrial transport defects and fragmentation in a time-dependent and pathway-specific manner

Fig. 2

Selective inhibition of fast transport of mitochondria by Aβ oligomers from human brain tissues. a Western blots (lower) showing the presence of small Aβ oligomers in the soluble fraction of brain homogenates from the three age- and sex-matched AD patients and control patients as indicated in the table above. Aβ monomers (1) and dimmers (2) were clearly seen, whereas trimmers (3) were only seen in one AD sample. b Quantitative analysis showing the selective impairment of mitochondrial transport by different dilutions of soluble AD homogenates in KRB. c Western blots showing the effective depletion of Aβ molecules by immunoprecipitation (IP). Two runs of IP were performed and the supernatants (Throu 1st and 2nd) and pellets (Output 1st and 2nd) were blotted. d Quantitative analysis showing the effects of the soluble AD brain homogenate (AD#2, Input) and its supernatant after immunoprecipitation (Throu 1st) on mitochondrial transport. Error bars are SD. *p < 0.05 and ** p < 0.005 (Student’s t-test). Ctrl: control; AD, AD brain sample, Throu: supernatant through IP; Mito: mitochondria; Endo/lyso: late endosomes/lysosomes. Each condition was repeated at least three times from different rounds of cultures and was averaged from 10–20 cells

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